Mimivirus TyrRS: Preliminary structural and functional characterization of the first amino-acyl tRNA synthetase found in a virus

Chantal Abergel, Sabine Chenivesse, Deborah Byrne, Karsten Suhre, Vincent Arondel, Jean Michel Claverie

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18 Citations (Scopus)

Abstract

The amoeba-infecting Mimivirus is the largest known double-stranded DNA virus, with a 400 nm particle size, comparable to that of mycoplasma. The complete sequence of its 1.2 Mbp genome has recently been determined [Raoult et al. (2004), Science, 306, 1344-1350] and revealed numerous genes that were not expected to be found in a virus, such as genes encoding translation components, including 4-amino-acyl tRNA synthetases and homologues to various translation initiation, elongation and termination factors. A comprehensive structural and functional study of these Mimivirus gene products was initiated, as they may hold important clues about the origin of DNA viruses. Here, the first preliminary crystallographic and functional results obtained on one of these targets, Mimivirus TyrRS, are reported. Preliminary phasing was obtained using an original combination of homology modelling and normal mode analysis. Experimental evidence that Mimivirus tyrosyl tRNA synthetase recombinant gene product does indeed activate tyrosine is also presented.

Original languageEnglish
Pages (from-to)212-215
Number of pages4
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume61
Issue number2
DOIs
Publication statusPublished - 1 Dec 2005

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ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics

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